泛素化和SUMO化对DEC1的拮抗调控作用

分化的胚软骨表达蛋白1(differentiated embryo-chondrocyte expressed gene 1,DEC1)作为一种时钟蛋白,除了在周期节律的调控中发挥转录抑制作用外,还在能量代谢以及多种肿瘤相关的信号通路的调控中发挥重要作用。此外,蛋白质的翻译后修饰是实现蛋白质功能精细调控的一种重要方式。目前发现,DEC1主要可被两种翻译后修饰,即泛素化和SUMO化修饰。尽管泛素化和SUMO化是两种过程非常类似的蛋白质翻译后修饰方式,但是它们对目的蛋白功能的调控却截然不同。由于泛素化和SUMO化与底物的作用靶点都是赖氨酸(Lys),因此在多数情况下,泛素化和SUMO化以拮抗性的方式调控底物蛋白的功能。鉴于此,该文旨在阐述泛素化和SUMO化修饰对DEC1功能的拮抗调节过程,为了解时钟蛋白DEC1对多种信号通路的调控过程中的分子机制提供新的思路。

The Antagonism Regulation of Ubiquitination and SUMOylation for DEC1

DEC1(differentiated embryo-chondrocyte expressed gene 1) is a clock protein which plays negative roles in regulation of circadian rhythm.Besides,DEC1 also takes important effect in metabolism and multi-tumor related signaling pathway.Moreover,post-translational modification is also an important regulation way to achieve the meticulous regulation of the protein functions.Recently,DEC1 could mainly be modified by two post-translational modifications–ubiquitination and SUMOylaiton.Although the processes of ubiquitination and SUMOylation are very similar,it is distinct in regulating the function of substrate proteins.Since the substrate target of both ubiquitination and SUMOylation is Lysine(Lys),it is usually ubiquitination and SUMOylation that antagonistly regulate the functions of substrate protein.Therefore,this article aims to describe the antagonism regulation of ubiquitination and SUMOylation for DEC1,which gives new insights into the molecular mechanism of clock protein DEC1 in regulating multi-signaling pathway.